Free Access
Issue
J. Chim. Phys.
Volume 96, Number 9/10, October/November/December 1999
Page(s) 1580 - 1584
DOI https://doi.org/10.1051/jcp:1999235
DOI: 10.1051/jcp:1999235


J. Chim. Phys. Vol. 96, N°9/10  p. 1580-1584

NMR studies of the R2 repeat and related peptide fragments of the DNA binding domain of c-Myb. New light on the structure and folding of R2.

I. Ségalas1, S. Desjardins1, H. Oulyadi1, Y. Prigent1, S. Tribouillard2, E. Bernardi2, A.R. Schoofs2, D. Davoust11 and F. Toma1

1  Laboratoire de RMN, UPRES-A 6014 du CNRS, IFRMP 23, Université de Rouen, IRCOF, 76821 Mont-Saint-Aignan, France
2  Centre Européen de Bioprospective, BP. 24, 76131 Mont-Saint-Aignan, France

Abstract
The solution structure of the R2 repeat of the DNA binding domain of the protooncogene c-Myb contains a N-terminal structural motif comprising two antiparallel helices. The motif is stabilized by interactions involving conserved residues. The recognition region in C-terminal position is flexible. This structure differs from that of R2 of another c-Myb protein.

Résumé
La structure en solution de la répétition R2 du domaine de liaison à l'ADN du protooncogène c-Myb possède un motif à deux hélices antiparallèles dans la moitié N-terminale, stabilisé par des interactions entre résidus conservés. La région de reconnaissance à l'ADN en position C-terminale est flexible. Cette structure diffère de celle montrée pour la répétition R2 d'une autre protéine c-Myb.


Key words: c-Myb -- protooncogene -- DNA binding -- structure -- NMR
Contents

© EDP Sciences 1999

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